The uniqueness of our methodologies derives from viewing protein structures as collections of points (e.g., atom coordinates, or points describing molecular surfaces) in 3D space, disregarding the order of the residues on the chains. Such computer-vision and robotics-based algorithms enable comparisons of protein surfaces, interfaces, or protein cores without being limited by the sequential order. Since the last site visit, we have made substantial progress in the development of new algorithms. Some of these (docking, and binding site comparison and detection) have already been described above. To enumerate the methods we have developed since the last site visit: residue-based multiple protein structure comparison (MultiProt; multiple alignment of proteins in their secondary structure representation (MASS); multiple alignment of protein structures in the functional group representation and of their binding sites (MultiBind), and of protein-protein interfaces (MAPPIS); SiteEngine, which carries out small molecule and protein-binding site recognition and I2ISiteEngine, which carries out pairwise structural comparisons of interfaces; flexible alignment of protein structures (FlexProt; Rigid body docking (PatchDock); Flexible hinge-bending docking (FlexDock); Symmetry docking (SymmDock; Combinatorial docking for folding and multimolecular assembly (CombDock); Prediction of binding sites using phage display libraries (SiteLight). In addition, using these, two nonredundant datasets of protein-protein interfaces have been assembled. The methods are all highly efficient with state of-the-art capabilities. I have already discussed the docking methods, SiteEngine and MAPPIS (Multiple Alignment of Protein-Protein InterfaceS). Below I briefly describe FlexProt, MASS and MultiProt. Most methods for multiple alignment start from the pairwise alignment solutions. In contrast, MASS and MultiProt derive multiple alignments from simultaneous superpositions of input molecules. Further, both methods do not require that all input molecules participate in the alignment. Actually, they efficiently detect high scoring partial multiple alignments for all possible number of molecules in the input. MASS (Multiple Alignment by Secondary Structures) and MultiProt (Multiple Proteins) are fully automated highly efficient techniques to detect multiple structural alignments of protein structures and detect common geometrical cores between input molecules. Furthermore, both methods are sequence-order independent. MASS is based on a two-level alignment, using both secondary structure and atomic representation. Utilizing secondary structure information aids in filtering out noisy solutions and achieves efficiency and robustness. MASS is capable of detecting nontopological structural motifs, where the secondary structures are arranged in a different order on the chains. Further, MASS is able to detect not only structural motifs, shared by all input molecules, but also motifs shared only by subsets of the molecules. We have demonstrated its ability to handle on the order of tens of molecules, to detect nontopological motifs and to find biologically meaningful alignments within nonpredefined subsets of the input. MASS is available at http://bioinfo3d.cs.tau.ac.il/MASS/. MultiProt considers protein structures as represented by points in space, where the points are either the C-alpha coordinates or the C-alpha and atoms or geometric center of the side chain. MultiProt is available at http://bioinfo3d.cs.tau.ac.il/MultiProt/. We have illustrated the power of both methods on a range of applications. The order-independence allows application of MultiProt to binding sites and protein-protein interfaces, making MultiProt an extremely useful structural tool. FlexProt is a novel technique for the alignment of flexible proteins. Unlike all previous algorithms to solve structural comparisons allowing hinge-bending motions, FlexProt does not require an a priori knowledge of the location of the hinge(s). FlexProt carries out the flexible alignment superimposing the matching rigid subpart pairs, and detects the flexible hinge regions simultaneously. Protein structural analysis requires algorithms that can deal with molecular flexibility. FlexProt efficiently detects maximal congruent rigid fragments in both molecules. Transforming the task into a graph theoretic problem, it calculates the optimal arrangement of previously detected maximal congruent rigid fragments. FlexProt performs a structural comparison of a pair of proteins 300 amino acids long in about seven seconds on a standard desktop PC. FlexProt can be accessed via the web at bioinfo3d.cs.tau.ac.il/FlexProt/. In addition, we have been developing a method to identify unpredefined tertiary structure of RNA using structural comparison techniques. We are applying it to the entire database of currently available RNA strucures (NMR and crystal) to derive a clustered nonredundant dataset or RNA tertiary structures. A newly started project also involves detection and mapping of channels and cavities inside protein structures